FHLA_ECOLI
ID FHLA_ECOLI Reviewed; 692 AA.
AC P19323; Q2MA98; Q47214;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Formate hydrogenlyase transcriptional activator FhlA;
GN Name=fhlA; OrderedLocusNames=b2731, JW2701;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2280686; DOI=10.1111/j.1365-2958.1990.tb00711.x;
RA Schlensog V., Boeck A.;
RT "Identification and sequence analysis of the gene encoding the
RT transcriptional activator of the formate hydrogenlyase system of
RT Escherichia coli.";
RL Mol. Microbiol. 4:1319-1327(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2118503; DOI=10.1128/jb.172.9.4798-4806.1990;
RA Maupin J.A., Shanmugam K.T.;
RT "Genetic regulation of formate hydrogenlyase of Escherichia coli: role of
RT the fhlA gene product as a transcriptional activator for a new regulatory
RT gene, fhlB.";
RL J. Bacteriol. 172:4798-4806(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12426353; DOI=10.1128/jb.184.23.6642-6653.2002;
RA Skibinski D.A., Golby P., Chang Y.S., Sargent F., Hoffman R., Harper R.,
RA Guest J.R., Attwood M.M., Berks B.C., Andrews S.C.;
RT "Regulation of the hydrogenase-4 operon of Escherichia coli by the
RT sigma(54)-dependent transcriptional activators FhlA and HyfR.";
RL J. Bacteriol. 184:6642-6653(2002).
CC -!- FUNCTION: Required for induction of expression of the formate
CC dehydrogenase H and hydrogenase-3 structural genes. Also activates
CC expression of hyf operon (encodes the silent hydrogenase-4 gene
CC cluster) (PubMed:12426353). {ECO:0000269|PubMed:12426353}.
CC -!- INTERACTION:
CC P19323; P0A6F5: groEL; NbExp=2; IntAct=EBI-1113147, EBI-543750;
CC -!- DISRUPTION PHENOTYPE: Loss of formate-inducible expression of the hyf
CC operon (PubMed:12426353). {ECO:0000269|PubMed:12426353}.
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DR EMBL; X52227; CAA36476.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69241.1; -; Genomic_DNA.
DR EMBL; M58504; AAA23770.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75773.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76808.1; -; Genomic_DNA.
DR PIR; S12079; S12079.
DR RefSeq; NP_417211.1; NC_000913.3.
DR RefSeq; WP_001301332.1; NZ_LN832404.1.
DR AlphaFoldDB; P19323; -.
DR SMR; P19323; -.
DR BioGRID; 4261423; 16.
DR BioGRID; 851513; 2.
DR IntAct; P19323; 4.
DR STRING; 511145.b2731; -.
DR jPOST; P19323; -.
DR PaxDb; P19323; -.
DR PRIDE; P19323; -.
DR EnsemblBacteria; AAC75773; AAC75773; b2731.
DR EnsemblBacteria; BAE76808; BAE76808; BAE76808.
DR GeneID; 947181; -.
DR KEGG; ecj:JW2701; -.
DR KEGG; eco:b2731; -.
DR PATRIC; fig|1411691.4.peg.4010; -.
DR EchoBASE; EB0297; -.
DR eggNOG; COG3604; Bacteria.
DR HOGENOM; CLU_000445_95_0_6; -.
DR InParanoid; P19323; -.
DR OMA; RMKRTID; -.
DR PhylomeDB; P19323; -.
DR BioCyc; EcoCyc:PD02936; -.
DR PRO; PR:P19323; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005667; C:transcription regulator complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00065; GAF; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; DNA-binding; Nucleotide-binding;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..692
FT /note="Formate hydrogenlyase transcriptional activator
FT FhlA"
FT /id="PRO_0000081297"
FT DOMAIN 202..344
FT /note="GAF"
FT DOMAIN 381..610
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 663..682
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 409..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 472..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT CONFLICT 39..49
FT /note="KRSALADNAAI -> NVLRRQRGY (in Ref. 2; AAA23770)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..71
FT /note="ASYYASREKDTPI -> RLISVACKRHPH (in Ref. 2; AAA23770)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="V -> L (in Ref. 2; AAA23770)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..333
FT /note="PYERMLFDTWGNQIQTLCLLPLMSGDTMLGVLKLAQCEEKVFTTTNLNLL
FT -> LRMSSTPGATDSNLVPVTADVWRHHAGRAETGANRRESVYHYQSEFT (in Ref.
FT 2; AAA23770)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="A -> R (in Ref. 2; AAA23770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 78468 MW; EB43989C92DFBA5A CRC64;
MSYTPMSDLG QQGLFDITRT LLQQPDLASL CEALSQLVKR SALADNAAIV LWQAQTQRAS
YYASREKDTP IKYEDETVLA HGPVRSILSR PDTLHCSYEE FCETWPQLDA GGLYPKFGHY
CLMPLAAEGH IFGGCEFIRY DDRPWSEKEF NRLQTFTQIV SVVTEQIQSR VVNNVDYELL
CRERDNFRIL VAITNAVLSR LDMDELVSEV AKEIHYYFDI DDISIVLRSH RKNKLNIYST
HYLDKQHPAH EQSEVDEAGT LTERVFKSKE MLLINLHERD DLAPYERMLF DTWGNQIQTL
CLLPLMSGDT MLGVLKLAQC EEKVFTTTNL NLLRQIAERV AIAVDNALAY QEIHRLKERL
VDENLALTEQ LNNVDSEFGE IIGRSEAMYS VLKQVEMVAQ SDSTVLILGE TGTGKELIAR
AIHNLSGRNN RRMVKMNCAA MPAGLLESDL FGHERGAFTG ASAQRIGRFE LADKSSLFLD
EVGDMPLELQ PKLLRVLQEQ EFERLGSNKI IQTDVRLIAA TNRDLKKMVA DREFRSDLYY
RLNVFPIHLP PLRERPEDIP LLAKAFTFKI ARRLGRNIDS IPAETLRTLS NMEWPGNVRE
LENVIERAVL LTRGNVLQLS LPDIVLPEPE TPPAATVVAL EGEDEYQLIV RVLKETNGVV
AGPKGAAQRL GLKRTTLLSR MKRLGIDKSA LI
